The Enzyme Database

Displaying entries 51-100 of 138.

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EC 3.5.1.51     
Accepted name: 4-acetamidobutyryl-CoA deacetylase
Reaction: 4-acetamidobutanoyl-CoA + H2O = acetate + 4-aminobutanoyl-CoA
Other name(s): aminobutyryl-CoA thiolesterase; deacetylase-thiolesterase
Systematic name: 4-acetamidobutanoyl-CoA amidohydrolase
Comments: The enzyme also hydrolyses 4-aminobutanoyl-CoA to aminobutanoate and coenzyme A.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ohsugi, M., Khan, J., Hensley, C., Chew, S. and Barker, H.A. Metabolism of L-β-lysine by a Pseudomonas. Purification and properties of a deacetylase-thiolesterase utilizing 4-acetamidobutyryl CoA and related compounds. J. Biol. Chem. 256 (1981) 7642–7651. [PMID: 6788773]
[EC 3.5.1.51 created 1984]
 
 
EC 3.5.1.52     
Accepted name: peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase
Reaction: Hydrolysis of an N4-(acetyl-β-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-β-D-glucosaminylamine and a peptide containing an aspartate residue
Other name(s): glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; Jack-bean glycopeptidase; PNGase A; PNGase F
Systematic name: N-linked-glycopeptide-(N-acetyl-β-D-glucosaminyl)-L-asparagine amidohydrolase
Comments: Does not act on (GlcNAc)Asn, because it requires the presence of more than two amino-acid residues in the substrate [cf. EC 3.5.1.26, N4-(β-N-acetylglucosaminyl)-L-asparaginase]. The plant enzyme was previously erroneously listed as EC 3.2.2.18.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 83534-39-8
References:
1.  Plummer, T.H., Jr. and Tarentino, A.L. Facile cleavage of complex oligosaccharides from glycopeptides by almond emulsin peptide: N-glycosidase. J. Biol. Chem. 256 (1981) 10243–10246. [PMID: 7287707]
2.  Takahashi, N. Demonstration of a new amidase acting on glycopeptides. Biochem. Biophys. Res. Commun. 76 (1977) 1194–1201. [DOI] [PMID: 901470]
3.  Takahashi, N. and Nishibe, H. Some characteristics of a new glycopeptidase acting on aspartylglycosylamine linkages. J. Biochem. (Tokyo) 84 (1978) 1467–1473. [PMID: 738997]
4.  Tarentino, A.L., Gomez, C.M. and Plummer, T.H., Jr. Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase F. Biochemistry 24 (1985) 4665–4671. [PMID: 4063349]
[EC 3.5.1.52 created 1984, modified 1989 (EC 3.2.2.18 created 1984, incorporated 1989)]
 
 
EC 3.5.1.53     
Accepted name: N-carbamoylputrescine amidase
Reaction: N-carbamoylputrescine + H2O = putrescine + CO2 + NH3
Glossary: putrescine = butane-1,4-diamine
Other name(s): carbamoylputrescine hydrolase; NCP
Systematic name: N-carbamoylputrescine amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 85030-69-9
References:
1.  Yanagisawa, H. and Suzuki, Y. Preparation and properties of N-carbamylputrescine amidohydrolase from maize shoots. Phytochemistry 21 (1982) 2201–2203.
[EC 3.5.1.53 created 1986]
 
 
EC 3.5.1.54     
Accepted name: allophanate hydrolase
Reaction: urea-1-carboxylate + H2O = 2 CO2 + 2 NH3
For diagram of atrazine catabolism, click here
Glossary: allophanate = urea-1-carboxylate
Other name(s): allophanate lyase; AtzF; TrzF
Systematic name: urea-1-carboxylate amidohydrolase
Comments: Along with EC 3.5.2.15 (cyanuric acid amidohydrolase) and EC 3.5.1.84 (biuret amidohydrolase), this enzyme forms part of the cyanuric-acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine], in bacteria. The yeast enzyme (but not that from green algae) also catalyses the reaction of EC 6.3.4.6, urea carboxylase, thus bringing about the hydrolysis of urea to CO2 and NH3 in the presence of ATP and bicarbonate. The enzyme from Pseudomonas sp. strain ADP has a narrow substrate specificity, being unable to use the structurally analogous compounds urea, hydroxyurea or methylcarbamate as substrate [6].
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9076-72-6
References:
1.  Maitz, G.S., Haas, E.M. and Castric, P.A. Purification and properties of the allophanate hydrolase from Chlamydomonas reinhardii. Biochim. Biophys. Acta 714 (1982) 486–491.
2.  Roon, R.J. and Levenberg, B. Urea amidolyase. I. Properties of the enzyme from Candida utilis. J. Biol. Chem. 247 (1972) 4107–4113. [PMID: 4556303]
3.  Sumrada, R.A. and Cooper, T.G. Urea carboxylase and allophanate hydrolase are components of a multifunctional protein in yeast. J. Biol. Chem. 257 (1982) 9119–9127. [PMID: 6124544]
4.  Kanamori, T., Kanou, N., Kusakabe, S., Atomi, H. and Imanaka, T. Allophanate hydrolase of Oleomonas sagaranensis involved in an ATP-dependent degradation pathway specific to urea. FEMS Microbiol. Lett. 245 (2005) 61–65. [DOI] [PMID: 15796980]
5.  Cheng, G., Shapir, N., Sadowsky, M.J. and Wackett, L.P. Allophanate hydrolase, not urease, functions in bacterial cyanuric acid metabolism. Appl. Environ. Microbiol. 71 (2005) 4437–4445. [DOI] [PMID: 16085834]
6.  Shapir, N., Sadowsky, M.J. and Wackett, L.P. Purification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp. strain ADP. J. Bacteriol. 187 (2005) 3731–3738. [DOI] [PMID: 15901697]
7.  Shapir, N., Cheng, G., Sadowsky, M.J. and Wackett, L.P. Purification and characterization of TrzF: biuret hydrolysis by allophanate hydrolase supports growth. Appl. Environ. Microbiol. 72 (2006) 2491–2495. [DOI] [PMID: 16597948]
[EC 3.5.1.54 created 1986, modified 2008]
 
 
EC 3.5.1.55     
Accepted name: long-chain-fatty-acyl-glutamate deacylase
Reaction: N-long-chain-fatty-acyl-L-glutamate + H2O = a long-chain carboxylate + L-glutamate
Other name(s): long-chain aminoacylase; long-chain-fatty-acyl-glutamate deacylase; long-chain acylglutamate amidase; N-acyl-D-glutamate deacylase
Systematic name: N-long-chain-fatty-acyl-L-glutamate amidohydrolase
Comments: Does not act on acyl derivates of other amino acids. Optimum chain length of acyl residue is 12 to 16.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 82249-69-2
References:
1.  Fukuda, H., Iwade, S. and Kimura, A. A new enzyme: long acyl aminoacylase from Pseudomonas diminuta. J. Biochem. (Tokyo) 91 (1982) 1731–1738. [PMID: 7096313]
[EC 3.5.1.55 created 1986]
 
 
EC 3.5.1.56     
Accepted name: N,N-dimethylformamidase
Reaction: N,N-dimethylformamide + H2O = dimethylamine + formate
Other name(s): dimethylformamidase; DMFase
Systematic name: N,N-dimethylformamide amidohydrolase
Comments: An iron protein. Also acts on N-ethylformamide and N-methyl-formamide and, more slowly, on N,N-diethylformamide, N,N-dimethylacetamide and unsubstituted acyl amides.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 104645-73-0
References:
1.  Schär, H.-P., Holzmann, W., Ramos Tombo, G.M. and Ghisalba, O. Purification and characterization of N,N-dimethylformamidase from Pseudomonas DMF 3/3. Eur. J. Biochem. 158 (1986) 469–475. [DOI] [PMID: 3732281]
[EC 3.5.1.56 created 1989]
 
 
EC 3.5.1.57     
Accepted name: tryptophanamidase
Reaction: L-tryptophanamide + H2O = L-tryptophan + NH3
Other name(s): tryptophan aminopeptidase; L-tryptophan aminopeptidase
Systematic name: L-tryptophanamide amidohydrolase
Comments: Requires Mn2+. Also acts on N-ethylformamide and L-tyrosinamide, and on some tryptophan dipeptides.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 76689-19-5
References:
1.  Iwayama, A., Kimura, T., Adachi, O. and Ameyama, M. Crystallization and characterization of a novel aminopeptidase from Trichosporon cutaneum. Agric. Biol. Chem. 47 (1983) 2483–2493.
[EC 3.5.1.57 created 1989]
 
 
EC 3.5.1.58     
Accepted name: N-benzyloxycarbonylglycine hydrolase
Reaction: N-benzyloxycarbonylglycine + H2O = benzyl alcohol + CO2 + glycine
Other name(s): benzyloxycarbonylglycine hydrolase; Nα-carbobenzoxyamino acid amidohydrolase; Nα-benzyloxycarbonyl amino acid urethane hydrolase; Nα-benzyloxycarbonyl amino acid urethane hydrolase I
Systematic name: N-benzyloxycarbonylglycine urethanehydrolase
Comments: Also acts, more slowly, on N-benzyloxycarbonylalanine, but not on the corresponding derivatives of other amino acids or on N-benzyloxycarbonylpeptides. Requires Co2+ or Zn2+. cf. EC 3.5.1.64, Nα-benzyloxycarbonylleucine hydrolase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 91930-69-7
References:
1.  Murao, S., Matsumura, E. and Kawano, T. Isolation and characterization of a novel enzyme, N α-benzyloxycarbonyl amino acid urethane hydrolase, from Streptococcus faecalis R ATCC 8043. Agric. Biol. Chem. 49 (1985) 967–972.
[EC 3.5.1.58 created 1989]
 
 
EC 3.5.1.59     
Accepted name: N-carbamoylsarcosine amidase
Reaction: N-carbamoylsarcosine + H2O = sarcosine + CO2 + NH3
For diagram of creatine biosynthesis, click here
Other name(s): carbamoylsarcosine amidase
Systematic name: N-carbamoylsarcosine amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 92767-52-7
References:
1.  Deeg, R., Roeder, A., Siedel, J., Gauhl, H. and Ziegenhorn, J. Process and reagent for the determination of N-carbamoylsarcosine with the use of a new enzyme. Patent DE3248145, Chem. Abstr. (1984), 101, 18751.
[EC 3.5.1.59 created 1989]
 
 
EC 3.5.1.60     
Accepted name: N-(long-chain-acyl)ethanolamine deacylase
Reaction: N-(long-chain-acyl)ethanolamine + H2O = a long-chain carboxylate + ethanolamine
Other name(s): NAAA (gene name); N-acylethanolamine amidohydrolase; acylethanolamine amidase
Systematic name: N-(long-chain-acyl)ethanolamine amidohydrolase
Comments: This lysosomal enzyme acts best on palmitoyl ethanolamide, with lower activity on other N-(long-chain-acyl)ethanolamines. It is only active at acidic pH. Unlike EC 3.5.1.99, fatty acid amide hydrolase, it does not act on primary amides such as oleamide, and has only a marginal activity with anandamide. The enzyme is translated as an inactive proenzyme, followed by autocatalytic cleavage into two subunits that reassociate to form an active heterodimeric complex.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 99283-61-1
References:
1.  Ueda, N., Yamanaka, K. and Yamamoto, S. Purification and characterization of an acid amidase selective for N-palmitoylethanolamine, a putative endogenous anti-inflammatory substance. J. Biol. Chem. 276 (2001) 35552–35557. [PMID: 11463796]
2.  Ueda, N., Yamanaka, K., Terasawa, Y. and Yamamoto, S. An acid amidase hydrolyzing anandamide as an endogenous ligand for cannabinoid receptors. FEBS Lett. 454 (1999) 267–270. [PMID: 10431820]
3.  West, J.M., Zvonok, N., Whitten, K.M., Wood, J.T. and Makriyannis, A. Mass spectrometric characterization of human N-acylethanolamine-hydrolyzing acid amidase. J. Proteome Res. 11 (2012) 972–981. [PMID: 22040171]
4.  Zhao, L.Y., Tsuboi, K., Okamoto, Y., Nagahata, S. and Ueda, N. Proteolytic activation and glycosylation of N-acylethanolamine-hydrolyzing acid amidase, a lysosomal enzyme involved in the endocannabinoid metabolism. Biochim. Biophys. Acta 1771 (2007) 1397–1405. [PMID: 17980170]
[EC 3.5.1.60 created 1989, modified 2019]
 
 
EC 3.5.1.61      
Transferred entry: mimosinase. Now EC 4.3.3.8, mimosinase
[EC 3.5.1.61 created 1989, deleted 2022]
 
 
EC 3.5.1.62     
Accepted name: acetylputrescine deacetylase
Reaction: N-acetylputrescine + H2O = acetate + putrescine
Glossary: putrescine = butane-1,4-diamine
spermidine = N-(3-aminopropyl)butane-1,4-diamine
Systematic name: N-acetylputrescine acetylhydrolase
Comments: The enzyme from Micrococcus luteus also acts on N8-acetylspermidine and acetylcadaverine, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 103679-48-7
References:
1.  Suzuki, O., Ishikawa, Y., Miyazaki, K., Izu, K. and Matsumoto, T. Acetylputrescine deacetylase from Micrococcus luteus K-11. Biochim. Biophys. Acta 882 (1986) 140–142.
[EC 3.5.1.62 created 1989]
 
 
EC 3.5.1.63     
Accepted name: 4-acetamidobutyrate deacetylase
Reaction: 4-acetamidobutanoate + H2O = acetate + 4-aminobutanoate
Glossary: 4-aminobutanoate = γ-aminobutyrate = GABA
Systematic name: 4-acetamidobutanoate amidohydrolase
Comments: Also acts on N-acetyl-β-alanine and 5-acetamidopentanoate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 102347-82-0
References:
1.  Haywood, G.W. and Large, P.J. 4-Acetamidobutyrate deacetylase in the yeast Candida boidinii grown on putrescine or spermidine as sole nitrogen source and its probable role in polyamine catabolism. J. Gen. Microbiol. 132 (1986) 7–14.
[EC 3.5.1.63 created 1989]
 
 
EC 3.5.1.64     
Accepted name: Nα-benzyloxycarbonylleucine hydrolase
Reaction: Nα-benzyloxycarbonyl-L-leucine + H2O = benzyl alcohol + CO2 + L-leucine
Other name(s): benzyloxycarbonylleucine hydrolase; Nα-benzyloxycarbonyl amino acid urethane hydrolase IV; α-N-benzyloxycarbonyl-L-leucine urethanehydrolase
Systematic name: Nα-benzyloxycarbonyl-L-leucine urethanehydrolase
Comments: Also acts on Nα-t-butoxycarbonyl-L-leucine, and, more slowly, on the corresponding derivatives of L-aspartate, L-methionine, L-glutamate and L-alanine. cf. EC 3.5.1.58 N-benzyloxycarbonylglycine hydrolase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 100630-47-5
References:
1.  Matsumura, E., Shin, T., Murao, S., Sakaguchi, M. and Kawano, T. A novel enzyme, Nα-benzyloxycarbonyl amino acid urethane hydrolase IV. Agric. Biol. Chem. 49 (1985) 3643–3645.
[EC 3.5.1.64 created 1989]
 
 
EC 3.5.1.65     
Accepted name: theanine hydrolase
Reaction: N5-ethyl-L-glutamine + H2O = L-glutamate + ethylamine
Glossary: L-theanine = N5-ethyl-L-glutamine
Other name(s): L-theanine amidohydrolase; 5-N-ethyl-L-glutamine amidohydrolase
Systematic name: N5-ethyl-L-glutamine amidohydrolase
Comments: Also acts on other N-alkyl-L-glutamines.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 99533-51-4
References:
1.  Tsushida, T. and Takeo, T. An enzyme hydrolyzing L-theanine in tea leaves. Agric. Biol. Chem. 49 (1985) 2913–2917.
[EC 3.5.1.65 created 1989]
 
 
EC 3.5.1.66     
Accepted name: 2-(hydroxymethyl)-3-(acetamidomethylene)succinate hydrolase
Reaction: 2-(hydroxymethyl)-3-(acetamidomethylene)succinate + 2 H2O = acetate + 2-(hydroxymethyl)-4-oxobutanoate + NH3 + CO2
Other name(s): compound B hydrolase; α-hydroxymethyl-α’-(N-acetylaminomethylene)succinic acid hydrolase
Systematic name: 2-(hydroxymethyl)-3-(acetamidomethylene)succinate amidohydrolase (deaminating, decarboxylating)
Comments: Involved in the degradation of pyridoxin by Pseudomonas and Arthrobacter.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 95829-26-8
References:
1.  Huynh, M.S. and Snell, E.E. Enzymes of vitamin B6 degradation. Purification and properties of two N-acetylamidohydrolases. J. Biol. Chem. 260 (1985) 2379–2383. [PMID: 3972793]
[EC 3.5.1.66 created 1989]
 
 
EC 3.5.1.67     
Accepted name: 4-methyleneglutaminase
Reaction: 4-methylene-L-glutamine + H2O = 4-methylene-L-glutamate + NH3
Other name(s): 4-methyleneglutamine deamidase; 4-methyleneglutamine amidohydrolase
Systematic name: 4-methylene-L-glutamine amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 86855-36-9
References:
1.  Ibrahim, S.A., Lea, P.J. and Fowden, L. Preparation and properties of 4-methyleneglutaminase from the leaves of peanut (Arachis hypogaea). Phytochemistry 23 (1984) 1545–1549.
[EC 3.5.1.67 created 1989]
 
 
EC 3.5.1.68     
Accepted name: N-formylglutamate deformylase
Reaction: N-formyl-L-glutamate + H2O = formate + L-glutamate
For diagram of histidine catabolism, click here
Other name(s): β-citryl-L-glutamate hydrolase; formylglutamate deformylase; N-formylglutamate hydrolase; β-citrylglutamate amidase; β-citryl-L-glutamate amidohydrolase; β-citryl-L-glutamate amidase; β-citryl-L-glutamate-hydrolyzing enzyme
Systematic name: N-formyl-L-glutamate amidohydrolase
Comments: The animal enzyme also acts on β-citryl-L-glutamate and β-citryl-L-glutamine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 97286-12-9
References:
1.  Hu, L., Mulfinger, L.M. and Phillips, A.T. Purification and properties of formylglutamate amidohydrolase from Pseudomonas putida. J. Bacteriol. 169 (1987) 4696–4702. [DOI] [PMID: 3308850]
2.  Miyake, M., Innami, T. and Kakimoto, Y. A β-citryl-L-glutamate-hydrolysing enzyme in rat testes. Biochim. Biophys. Acta 760 (1983) 206–214. [DOI] [PMID: 6414521]
[EC 3.5.1.68 created 1989]
 
 
EC 3.5.1.69     
Accepted name: glycosphingolipid deacylase
Reaction: Hydrolysis of gangliosides and neutral glycosphingolipids, releasing fatty acids to form the lyso-derivatives
Other name(s): glycosphingolipid ceramide deacylase
Systematic name: glycosphingolipid amidohydrolase
Comments: Does not act on sphingolipids such as ceramide. Not identical with EC 3.5.1.23 ceramidase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 122544-53-0
References:
1.  Hirabayashi, Y., Kimura, M., Matsumoto, M., Yamamoto, K., Kadowaki, S. and Tochikura, T. A novel glycosphingolipid hydrolyzing enzyme, glycosphingolipid ceramide deacylase, which cleaves the linkage between the fatty acid and sphingosine base in glycosphingolipids. J. Biochem. (Tokyo) 103 (1988) 1–4. [PMID: 3360750]
[EC 3.5.1.69 created 1990]
 
 
EC 3.5.1.70     
Accepted name: aculeacin-A deacylase
Reaction: Hydrolysis of the amide bond in aculeacin A and related neutral lipopeptide antibiotics, releasing the long-chain fatty acid side-chain
Other name(s): aculeacin A acylase
Systematic name: aculeacin-A amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 121479-50-3
References:
1.  Takeshima, H., Inokoshi, J., Takada, Y., Tanaka, H. and Omura, S. A deacylation enzyme for aculeacin A, a neutral lipopeptide antibiotic, from Actinoplanes utahensis: purification and characterization. J. Biochem. (Tokyo) 105 (1989) 606–610. [PMID: 2760018]
[EC 3.5.1.70 created 1992]
 
 
EC 3.5.1.71     
Accepted name: N-feruloylglycine deacylase
Reaction: N-feruloylglycine + H2O = ferulate + glycine
Other name(s): N-feruloylglycine hydrolase
Systematic name: N-feruloylglycine amidohydrolase
Comments: Hydrolyses a range of L-amino acids from the cinnamoyl and substituted cinnamoyl series. Not identical with EC 3.5.1.14 aminoacylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 118731-84-3
References:
1.  Martens, M., Cottenie-Ruysschaert, M., Hanselaer, R., De Cooman, L., Casteele, K.V. and Van Sumere, F. N-Feruloylglycine amidohydrolase from barley seeds and isolated barley embryos. Phytochemistry 27 (1988) 2457–2463.
2.  Martens, M., Cottenie-Ruysschaert, M., Hanselaer, R., De Cooman, L., Casteele, K.V. and Van Sumere, F. Characteristics and specificity of purified N-feruloylglycine amidohydrolase from isolated barley embryos. Phytochemistry 27 (1988) 2465–2475.
[EC 3.5.1.71 created 1992]
 
 
EC 3.5.1.72     
Accepted name: D-benzoylarginine-4-nitroanilide amidase
Reaction: N-benzoyl-D-arginine-4-nitroanilide + H2O = N-benzoyl-D-arginine + 4-nitroaniline
Other name(s): benzoyl-D-arginine arylamidase; D-BAPA-ase
Systematic name: N-benzoyl-D-arginine-4-nitroanilide amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 119345-26-5
References:
1.  Gofshtein-Gandman, L.V., Keynan, A. and Milner, Y. Bacteria of the genus Bacillus have a hydrolase stereospecific to the D isomer of benzoyl-arginine-p-nitroanilide. J. Bacteriol. 170 (1988) 5895–5900. [DOI] [PMID: 3142860]
[EC 3.5.1.72 created 1992]
 
 
EC 3.5.1.73     
Accepted name: carnitinamidase
Reaction: L-carnitinamide + H2O = L-carnitine + NH3
Other name(s): L-carnitinamidase; carnitine amidase; L-carnitine amidase
Systematic name: L-carnitinamide amidohydrolase
Comments: Does not act on D-carnitinamide.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 117444-04-9
References:
1.  Nakayama, K., Honda, H., Ogawa, Y., Ozawa, T. and Ota, T. Method for producing carnitine, L- carnitinamide hydrolase and method for producing same. Patent DE3728321, Chem. Abstr. (1988), 109, 22873.
[EC 3.5.1.73 created 1992]
 
 
EC 3.5.1.74     
Accepted name: chenodeoxycholoyltaurine hydrolase
Reaction: chenodeoxycholoyltaurine + H2O = chenodeoxycholate + taurine
Glossary: chenodeoxycholate = 3α,7α-dihydroxy-5β-cholan-24-oate
Systematic name: chenodeoxycholoyltaurine amidohydrolase
Comments: Some other taurine conjugates are hydrolysed, but not glycine conjugates of bile acids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 125752-75-2
References:
1.  Kawamoto, K., Horibe, I. and Uchida, K. Purification and characterization of a new hydrolase for conjugated bile acids, chenodeoxycholyltaurine hydrolase, from Bacteroides vulgatus. J. Biochem. (Tokyo) 106 (1989) 1049–1053. [PMID: 2628421]
[EC 3.5.1.74 created 1992]
 
 
EC 3.5.1.75     
Accepted name: urethanase
Reaction: urethane + H2O = ethanol + CO2 + NH3
Other name(s): urethane hydrolase
Systematic name: urethane amidohydrolase (decarboxylating)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 122007-70-9
References:
1.  Kobashi, K., Takebe, S. and Sakai, T. Urethane-hydrolyzing enzyme from Citrobacter sp. Chem. Pharm. Bull. 38 (1990) 1326–1328. [PMID: 2393957]
[EC 3.5.1.75 created 1992]
 
 
EC 3.5.1.76     
Accepted name: arylalkyl acylamidase
Reaction: N-acetylarylalkylamine + H2O = arylalkylamine + acetate
Other name(s): aralkyl acylamidase
Systematic name: N-acetylarylalkylamine amidohydrolase
Comments: Identified in Pseudomonas putida. Strict specificity for N-acetyl arylalkylamines, including N-acetyl-2-phenylethylamine, N-acetyl-3-phenylpropylamine, N-acetyldopamine, N-acetyl-serotonin and melatonin. It also accepts arylalkyl acetates but not acetanilide derivatives, which are common substrates of EC 3.5.1.13, aryl acylamidase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Shimizu, S., Ogawa, J., Chung, M.C.-M., Yamada, H. Purification and characterization of a novel enzyme, arylalkyl acylamidase, from Pseudomonas putida Sc2. Eur. J. Biochem. 209 (1992) 375–382. [DOI] [PMID: 1396711]
[EC 3.5.1.76 created 1999]
 
 
EC 3.5.1.77     
Accepted name: N-carbamoyl-D-amino-acid hydrolase
Reaction: an N-carbamoyl-D-amino acid + H2O = a D-amino acid + NH3 + CO2
Other name(s): D-N-carbamoylase; N-carbamoylase (ambiguous); N-carbamoyl-D-amino acid hydrolase
Systematic name: N-carbamoyl-D-amino-acid amidohydrolase
Comments: This enzyme, along with EC 3.5.1.87 (N-carbamoyl-L-amino-acid hydrolase), EC 5.1.99.5 (hydantoin racemase) and hydantoinase, forms part of the reaction cascade known as the "hydantoinase process", which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids [2]. It has strict stereospecificity for N-carbamoyl-D-amino acids and does not act upon the corresponding L-amino acids or on the N-formyl amino acids, N-carbamoyl-sarcosine, -citrulline, -allantoin and -ureidopropanoate, which are substrates for other amidohydrolases.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 71768-08-6
References:
1.  Ogawa, J., Shimizu, S., Yamada, H. N-Carbamoyl-D-amino acid amidohydrolase from Comamonas sp. E222c; purification and characterization. Eur. J. Biochem. 212 (1993) 685–691. [DOI] [PMID: 8462543]
2.  Altenbuchner, J., Siemann-Herzberg, M. and Syldatk, C. Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids. Curr. Opin. Biotechnol. 12 (2001) 559–563. [DOI] [PMID: 11849938]
[EC 3.5.1.77 created 1999, modified 2008]
 
 
EC 3.5.1.78     
Accepted name: glutathionylspermidine amidase
Reaction: glutathionylspermidine + H2O = glutathione + spermidine
For diagram of trypanothione biosynthesis, click here
Glossary: spermidine = N-(3-aminopropyl)butane-1,4-diamine
Other name(s): glutathionylspermidine amidohydrolase (spermidine-forming)
Systematic name: γ-L-glutamyl-L-cysteinyl-glycine:spermidine amidase
Comments: Spermidine is numbered so that atom N-1 is in the amino group of the aminopropyl part of the molecule. The enzyme from Escherichia coli is bifunctional and also catalyses the glutathionylspermidine synthase (EC 6.3.1.8) reaction, resulting in a net hydrolysis of ATP.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 171040-71-4
References:
1.  Bollinger, J.M., Kwon, D.S., Huisman, G.W., Kolter, R., Walsh, C.T. Glutathionylspermidine metabolism in E. coli. Purification, cloning, overproduction and characterization of a bifunctional glutathionylspermidine synthetase/amidase. J. Biol. Chem. 270 (1995) 14031–14041. [DOI] [PMID: 7775463]
[EC 3.5.1.78 created 1999]
 
 
EC 3.5.1.79     
Accepted name: phthalyl amidase
Reaction: a phthalylamide + H2O = phthalic acid + a substituted amine
Systematic name: phthalyl-amide amidohydrolase
Comments: In the entry, "phthalyl" is used to mean "2-carboxybenzoyl". The enzyme from Xanthobacter agilis hydrolyses phthalylated amino acids, peptides, β-lactams, aromatic and aliphatic amines. The substituent on nitrogen may be an alkyl group, but may also be complex, giving an amino acid or peptide derivative. Substitutions on the phthalyl ring include 6-F, 6-NH2, 3-OH, and a nitrogen in the aromatic ring ortho to the carboxy group attached to the amine. No cofactors are required
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 169150-79-2
References:
1.  Briggs, B.S., Kreuzman, A.J., Whitesitt, C., Yeh, W.K., Zmijewski, M. Discovery, purification, and properties of o-phthalyl amidase from Xanthobacter agilis. J. Mol. Catal., B Enzym. 2 (1996) 53–69.
2.  Black, T.D., Briggs, B.S., Evans, R., Muth, W.L., Vangala, S., Zmijewski, M.J. o-Phthalyl amidase in the synthesis of Loracarbef: process development using this novel biocatalyst. Biotechnol. Lett. 18 (1996) 875–880.
3.  Costello, C., Kreuzman, A., Zmijewski, M. Selective deprotection of phthalyl protected proteins. Tetrahedron Lett. 37 (1996) 7469–7472.
4.  Briggs, B.S., Zmijewski, M.J. Enzyme from microbial source: phthalyl amidase. Patent US5445959, Chem. Abstr. (1995), 123, 25010 (PDF).
[EC 3.5.1.79 created 1999]
 
 
EC 3.5.1.80      
Deleted entry: N-acetylgalactosamine-6-phosphate deacetylase. Identical to EC 3.5.1.25, N-acetylglucosamine-6-phosphate deacetylase
[EC 3.5.1.80 created 1999, deleted 2002]
 
 
EC 3.5.1.81     
Accepted name: N-acyl-D-amino-acid deacylase
Reaction: N-acyl-D-amino acid + H2O = a carboxylate + D-amino acid
Systematic name: N-acyl-D-amino acid amidohydrolase
Comments: The enzyme from Alcaligenes denitrificans subsp. xylosoxydans and Alcaligenes xylosoxydans subsp. xylosoxydans has wide specificity; hydrolyses N-acyl derivative of neutral D-amino acids. Used in separating D- and L-amino acids. Requires zinc.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 65979-42-2
References:
1.  Wakayama, M., Katsuno, Y., Hayashi, S., Miyamoto, Y., Sakai, K., Moriguchi, M. Cloning and sequencing of a gene encoding D-aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6 and expression of the gene in Escherichia coli. Biosci. Biotechnol. Biochem. 59 (1995) 2115–2119. [DOI] [PMID: 8541651]
2.  Wakayama, M., Hayashi, S., Yatsuda, Y., Katsuno, Y., Sakai, K. and Moriguchi, M. Overproduction of D-aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6 in Escherichia coli and its purification. Protein Expr. Purif. 7 (1996) 395–399. [DOI] [PMID: 8776758]
[EC 3.5.1.81 created 1999]
 
 
EC 3.5.1.82     
Accepted name: N-acyl-D-glutamate deacylase
Reaction: N-acyl-D-glutamate + H2O = a carboxylate + D-glutamate
Systematic name: N-acyl-D-glutamate amidohydrolase
Comments: The enzyme from Alcaligenes xylosoxydans subsp. xylosoxydans and Pseudomonas sp. is specific for N-acyl-D-glutamate. Requires zinc.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 82249-69-2
References:
1.  Wakayama, M., Ashika, T., Miyamoto, Y., Yoshikawa, T., Sonoda, Y., Sakai, K. and Moriguchi, M. Primary structure of N-acyl-D-glutamate amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6. J. Biochem. (Tokyo) 118 (1995) 204–209. [PMID: 8537313]
2.  Wakayama, M., Miura, Y., Oshima, K., Sakai, K., Moriguchi, M. Metal-characterization of N-acyl-D-glutamate amidohydrolase from Pseudomonas sp. strain 5f-1. Biosci. Biotechnol. Biochem. 59 (1995) 1489–1492. [DOI] [PMID: 7549100]
3.  Wakayama, M., Tsutsumi, T., Yada, H., Sakai, K., Moriguchi, M. Chemical modification of histidine residue of N-acyl-D-glutamate amidohydrolase from Pseudomonas sp. 5f-1. Biosci. Biotechnol. Biochem. 60 (1996) 650–653. [DOI] [PMID: 8829533]
[EC 3.5.1.82 created 1999]
 
 
EC 3.5.1.83     
Accepted name: N-acyl-D-aspartate deacylase
Reaction: N-acyl-D-aspartate + H2O = a carboxylate + D-aspartate
Systematic name: N-acyl-D-aspartate amidohydrolase
Comments: The enzyme from Alcaligenes xylosoxydans subsp. xylosoxydans is specific for N-acyl-D-aspartate. Requires zinc.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9031-86-1
References:
1.  Moriguchi, M., Sakai, K., Katsuno, Y., Maki, T., Wakayama, M. Purification and characterization of novel N-acyl-D-aspartate amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6. Biosci. Biotechnol. Biochem. 57 (1993) 1145–1148. [DOI] [PMID: 7763985]
2.  Wakayama, M., Watanabe, E., Takenaka, Y., Miyamoto, Y., Tau, Y., Sakai, K., Moriguchi, M. Cloning, expression and nucleotide sequence of the N-acyl-D-aspartate amidohydrolase gene from Alcaligenes xylosoxydans subsp. xylosoxydans A-6. J. Ferment. Bioeng. 80 (1995) 311–317.
[EC 3.5.1.83 created 1999]
 
 
EC 3.5.1.84     
Accepted name: biuret amidohydrolase
Reaction: biuret + H2O = urea-1-carboxylate + NH3
For diagram of atrazine catabolism, click here
Glossary: biuret = imidodicarbonic diamide
allophanate = urea-1-carboxylate
Other name(s): biuH (gene name)
Systematic name: biuret amidohydrolase
Comments: The enzyme, characterized from the bacterium Rhizobium leguminosarum bv. viciae 3841, participates in the degradation of cyanuric acid, an intermediate in the degradation of s-triazide herbicides such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine]. The substrate, biuret, forms by the spontaneous decarboxylation of 1-carboxybiuret in the absence of EC 3.5.1.131, 1-carboxybiuret hydrolase.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 95567-88-7
References:
1.  Cameron, S.M., Durchschein, K., Richman, J.E., Sadowsky, M.J. and Wackett, L.P. A new family of biuret hydrolases involved in s-triazine ring metabolism. ACS Catal. 2011 (2011) 1075–1082. [PMID: 21897878]
2.  Esquirol, L., Peat, T.S., Wilding, M., Lucent, D., French, N.G., Hartley, C.J., Newman, J. and Scott, C. Structural and biochemical characterization of the biuret hydrolase (BiuH) from the cyanuric acid catabolism pathway of Rhizobium leguminosarum bv. viciae 3841. PLoS One 13:e0192736 (2018). [PMID: 29425231]
3.  Esquirol, L., Peat, T.S., Wilding, M., Liu, J.W., French, N.G., Hartley, C.J., Onagi, H., Nebl, T., Easton, C.J., Newman, J. and Scott, C. An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. J. Biol. Chem. 293 (2018) 7880–7891. [DOI] [PMID: 29523689]
[EC 3.5.1.84 created 2000, modified 2008, modified 2019]
 
 
EC 3.5.1.85     
Accepted name: (S)-N-acetyl-1-phenylethylamine hydrolase
Reaction: N-acetylphenylethylamine + H2O = phenylethylamine + acetate
Systematic name: (S)-N-acetylphenylethylamine:H2O hydrolase
Comments: Inhibited by phenylmethanesulfonyl fluoride. Some related acetylated compounds are hydrolysed with variable enantiomeric selectivities.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 192230-94-7
References:
1.  Brunella, A., Graf, M., Kittelmann, M., Lauma, K. and Ghisalba, O. Production, purification, and characterization of a highly enantioselective (S)-N-acetyl-1-phenylethyl amidohydrolase from Rhodococcus. Appl. Microbiol. Biotechnol. 47 (1997) 515–520.
[EC 3.5.1.85 created 2000, modified 2002]
 
 
EC 3.5.1.86     
Accepted name: mandelamide amidase
Reaction: (R)-mandelamide + H2O = (R)-mandelate + NH3
Glossary: (R)-mandelate = (R)-2-hydroxy-2-phenylacetate
Other name(s): Pseudomonas mandelamide hydrolase
Systematic name: mandelamide hydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yamamoto, K., Oishi, K., Fujimatsu, I. and Komatsu, K. Production of R-(-)-mandelic acid from mandelonitrile by Alcaligenes faecalis ATCC 8750. Appl. Environ. Microbiol. 57 (1991) 3028–3032. [PMID: 1660699]
[EC 3.5.1.86 created 2000]
 
 
EC 3.5.1.87     
Accepted name: N-carbamoyl-L-amino-acid hydrolase
Reaction: an N-carbamoyl-L-2-amino acid (a 2-ureido carboxylate) + H2O = an L-2-amino acid + NH3 + CO2
Other name(s): N-carbamyl L-amino acid amidohydrolase; N-carbamoyl-L-amino acid amidohydrolase; L-N-carbamoylase; N-carbamoylase (ambiguous)
Systematic name: N-carbamoyl-L-amino-acid amidohydrolase
Comments: This enzyme, along with EC 3.5.1.77 (N-carbamoyl-D-amino-acid hydrolase), EC 5.1.99.5 (hydantoin racemase) and hydantoinase, forms part of the reaction cascade known as the "hydantoinase process", which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids [3]. The enzyme from Alcaligenes xylosoxidans has broad specificity for carbamoyl-L-amino acids, although it is inactive on the carbamoyl derivatives of glutamate, aspartate, arginine, tyrosine or tryptophan. The enzyme from Sinorhizobium meliloti requires a divalent cation for activity and can hydrolyse N-carbamoyl-L-tryptophan as well as N-carbamoyl L-amino acids with aliphatic substituents [2]. The enzyme is inactive on derivatives of D-amino acids. In addition to N-carbamoyl L-amino acids, the enzyme can also hydrolyse formyl and acetyl derivatives to varying degrees [1,2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Ogawa, J., Miyake, H. and Shimizu, S. Purification and characterization of N-carbamoyl-L-amino acid amidohydrolase with broad substrate specificity from Alcaligenes xylosoxidans. Appl. Microbiol. Biotechnol. 43 (1995) 1039–1043. [PMID: 8590654]
2.  Martínez-Rodríguez, S., Clemente-Jiménez, J.M., Rodríguez-Vico, F. and Las Heras-Vázquez, F.J. Molecular cloning and biochemical characterization of L-N-carbamoylase from Sinorhizobium meliloti CECT4114. J. Mol. Microbiol. Biotechnol. 9 (2005) 16–25. [DOI] [PMID: 16254442]
3.  Altenbuchner, J., Siemann-Herzberg, M. and Syldatk, C. Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids. Curr. Opin. Biotechnol. 12 (2001) 559–563. [DOI] [PMID: 11849938]
[EC 3.5.1.87 created 2001, modified 2008]
 
 
EC 3.5.1.88     
Accepted name: peptide deformylase
Reaction: formyl-L-methionyl peptide + H2O = formate + methionyl peptide
Other name(s): N-formylmethionylaminoacyl-tRNA deformylase
Systematic name: formyl-L-methionyl peptide amidohydrolase
Comments: Requires iron(II). Also requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Differs in substrate specifity from EC 3.5.1.31 (formylmethionine deformylase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 369636-51-1
References:
1.  Adams, J.M. On the release of the formyl group from nascent protein. J. Mol. Biol. 33 (1968) 571–589. [DOI] [PMID: 4973445]
2.  Mazel, D., Pochet, S. and Marliere, P. Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation. EMBO J. 13 (1994) 914–923. [PMID: 8112305]
3.  Chan, M.K., Gong, W., Rajagopalan, P.T.R., Hao, B., Tsai, C.M. and Pei, D. Crystal structure of the Escherichia coli peptide deformylase. Biochemistry 36 (1997) 13904–13909. [DOI] [PMID: 9374869]
4.  Becker, A., Schlichting, I., Kabsch, W., Schultz, S. and Wagner, A.F.V. Structure of peptide deformylase and identification of the substrate binding site. J. Biol. Chem. 273 (1998) 11413–11416. [DOI] [PMID: 9565550]
5.  Becker, A., Schlichting, I., Kabsch, W., Groche, D., Schultz, S. and Wagner, A.F. Iron center, substrate recognition, and mechanism of peptide deformylase. Nat. Struct. Biol. 5 (1998) 1053–1058. [DOI] [PMID: 9846875]
6.  Rajagopalan, P.T.R., Yu, X.C. and Pei, D. Peptide deformylase: a new type of mononuclear iron protein. J. Am. Chem. Soc. 119 (1997) 12418–12419.
7.  Groche, D., Becker, A., Schlichting, I., Kabsch, W., Schultz, S. and Wagner, A.F.V. Isolation and crystallization of functionally competent Escherichia coli peptide deformylase forms containing either iron or nickel in the active site. Biochem. Biophys. Res. Commun. 246 (1998) 342–346. [DOI] [PMID: 9610360]
8.  Rajagopalan, P.T.R., Grimme, S. and Pei, D. Characterization of cobalt(II)-substituted peptide deformylase: function of the metal ion and the catalytic residue Glu-133. Biochemistry 39 (2000) 779–790. [DOI] [PMID: 10651644]
9.  Hu, Y.J., Wei, Y., Zhou, Y., Rajagopalan, P.T.R. and Pei, D. Determination of substrate specificity for peptide deformylase through the screening of a combinatorial peptide library. Biochemistry 38 (1999) 643–650. [DOI] [PMID: 9888804]
10.  Ragasu, S., Mouchet, P., Lazennec, C., Dive, V. and Meinnel, T. Substrate recognition and selectivity of peptide deformylase. Similarities and differences with metzincins and thermolysin. J. Mol. Biol. 289 (1999) 1445–1457. [DOI] [PMID: 10373378]
11.  Giglione, C., Pierre, M. and Meinnel, T. Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents. Mol. Microbiol. 36 (2000) 1197–1205. [DOI] [PMID: 10931273]
12.  Pei, D. Peptide deformylase: a target for novel antibiotics? Emerging Therapeutic Targets 5 (2001) 23–40. [DOI] [PMID: 15992166]
[EC 3.5.1.88 created 2001]
 
 
EC 3.5.1.89     
Accepted name: N-acetylglucosaminylphosphatidylinositol deacetylase
Reaction: 6-(N-acetyl-α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
For diagram of glycosylphosphatidyl-myo-inositol biosynthesis, click here
Other name(s): N-acetyl-D-glucosaminylphosphatidylinositol acetylhydrolase; N-acetylglucosaminylphosphatidylinositol de-N-acetylase; GlcNAc-PI de-N-acetylase; GlcNAc-PI deacetylase; acetylglucosaminylphosphatidylinositol deacetylase
Systematic name: 6-(N-acetyl-α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol acetylhydrolase
Comments: Involved in the second step of glycosylphosphatidylinositol (GPI) anchor formation in all eukaryotes. The enzyme appears to be composed of a single subunit (PIG-L in mammalian cells and GPI12 in yeast). In some species, the long-chain sn-1-acyl group of the phosphatidyl group is replaced by a long-chain alkyl or alk-1-enyl group.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 122191-30-4
References:
1.  Doering, T.L., Masteron, W.J., Englund, P.T. and Hart, G.W. Biosynthesis of the glycosyl phosphatidylinositol membrane anchor of the trypanosome variant surface glycoprotein. Origin of the non-acetylated glucosamine. J. Biol. Chem. 264 (1989) 11168–11173. [PMID: 2525555]
2.  Nakamura, N., Inoue, N., Watanabe, R., Takahashi, M., Takeda, J., Stevens, V.L. and Kinoshita, T. Expression cloning of PIG-L, a candidate N-acetylglucosaminyl-phosphatidylinositol deacetylase. J. Biol. Chem. 272 (1997) 15834–15840. [DOI] [PMID: 9188481]
3.  Watanabe, R., Ohishi, K., Maeda, Y., Nakamura, N. and Kinoshita, T. Mammalian PIG-L and its yeast homologue Gpi12p are N-acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis. Biochem. J. 339 (1999) 185–192. [PMID: 10085243]
4.  Smith, T.K, Crossman, A., Borissow, C.N., Paterson, M.J., Dix, A., Brimacombe, J.S. and Ferguson, M.A.J. Specificity of GlcNAc-PI de-N-acetylase of GPI biosynthesis and synthesis of parasite-specific suicide substrate inhibitors. EMBO J. 20 (2001) 3322–3332. [DOI] [PMID: 11432820]
[EC 3.5.1.89 created 1992 as EC 3.1.1.69, transferred 2002 to EC 3.5.1.89, modified 2002]
 
 
EC 3.5.1.90     
Accepted name: adenosylcobinamide hydrolase
Reaction: adenosylcobinamide + H2O = adenosylcobyric acid + (R)-1-aminopropan-2-ol
For diagram of cobinamide salvage pathways, click here
Other name(s): CbiZ; AdoCbi amidohydrolase
Systematic name: adenosylcobinamide amidohydrolase
Comments: Involved in the salvage pathway of cobinamide in archaea. Archaea convert adenosylcobinamide (AdoCbi) into adenosylcobinamide phosphate (AdoCbi-P) in two steps. First, the amidohydrolase activity of CbiZ cleaves off the aminopropanol moiety of AdoCbi yielding adenosylcobyric acid (AdoCby); second, AdoCby is converted into AdoCbi-P by the action of EC 6.3.1.10, adenosylcobinamide-phosphate synthase (CbiB).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 905988-16-1
References:
1.  Woodson, J.D. and Escalante-Semerena, J.C. CbiZ, an amidohydrolase enzyme required for salvaging the coenzyme B12 precursor cobinamide in archaea. Proc. Natl. Acad. Sci. USA 101 (2004) 3591–3596. [DOI] [PMID: 14990804]
[EC 3.5.1.90 created 2004]
 
 
EC 3.5.1.91     
Accepted name: N-substituted formamide deformylase
Reaction: N-benzylformamide + H2O = formate + benzylamine
For diagram of reaction, click here
Other name(s): NfdA
Systematic name: N-benzylformamide amidohydrolase
Comments: Zinc is a cofactor. While N-benzylformamide is the best substrate, the enzyme from Arthrobacter pascens can also act on the N-substituted formamides N-butylformamide, N-allylformamide, N-[2-(cyclohex-1-enyl)ethyl]formamide and N-(1-phenylethyl)formamide, but much more slowly. Amides of other acids do not act as substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 115299-95-1
References:
1.  Fukatsu, H., Hashimoto, Y., Goda, M., Higashibata, H. and Kobayashi, M. Amine-synthesizing enzyme N-substituted formamide deformylase: screening, purification, characterization, and gene cloning. Proc. Natl. Acad. Sci. USA 101 (2004) 13726–13731. [DOI] [PMID: 15358859]
[EC 3.5.1.91 created 2005]
 
 
EC 3.5.1.92     
Accepted name: pantetheine hydrolase
Reaction: (R)-pantetheine + H2O = (R)-pantothenate + 2-aminoethanethiol
Other name(s): pantetheinase; vanin; vanin-1
Systematic name: (R)-pantetheine amidohydrolase
Comments: The enzyme hydrolyses only one of the amide bonds of pantetheine. The substrate analogues phosphopantetheine and CoA are not substrates. The enzyme recycles pantothenate (vitamin B5) and produces 2-aminoethanethiol (cysteamine), a potent anti-oxidant [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 56093-18-6
References:
1.  Duprè, S. and Cavallini, D. Purification and properties of pantetheinase from horse kidney. Methods Enzymol. 62 (1979) 262–267. [PMID: 440106]
2.  Duprè, S., Chiaraluce, R., Nardini, M., Cannella, C., Ricci, G. and Cavallini, D. Continuous spectrophotometric assay of pantetheinase activity. Anal. Biochem. 142 (1984) 175–181. [DOI] [PMID: 6549111]
3.  Maras, B., Barra, D., Duprè, S. and Pitari, G. Is pantetheinase the actual identity of mouse and human vanin-1 proteins? FEBS Lett. 461 (1999) 149–152. [DOI] [PMID: 10567687]
4.  Aurrand-Lions, M., Galland, F., Bazin, H., Zakharyev, V.M., Imhof, B.A. and Naquet, P. Vanin-1, a novel GPI-linked perivascular molecule involved in thymus homing. Immunity 5 (1996) 391–405. [DOI] [PMID: 8934567]
5.  Pitari, G., Malergue, F., Martin, F., Philippe, J.M., Massucci, M.T., Chabret, C., Maras, B., Duprè, S., Naquet, P. and Galland, F. Pantetheinase activity of membrane-bound Vanin-1: lack of free cysteamine in tissues of Vanin-1 deficient mice. FEBS Lett. 483 (2000) 149–154. [DOI] [PMID: 11042271]
6.  Martin, F., Malergue, F., Pitari, G., Philippe, J.M., Philips, S., Chabret, C., Granjeaud, S., Mattei, M.G., Mungall, A.J., Naquet, P. and Galland, F. Vanin genes are clustered (human 6q22-24 and mouse 10A2B1) and encode isoforms of pantetheinase ectoenzymes. Immunogenetics 53 (2001) 296–306. [PMID: 11491533]
7.  Pace, H.C. and Brenner, C. The nitrilase superfamily: classification, structure and function. Genome Biol. 2 (2001) 0001.. [PMID: 11380987]
[EC 3.5.1.92 created 2006]
 
 
EC 3.5.1.93     
Accepted name: glutaryl-7-aminocephalosporanic-acid acylase
Reaction: (7R)-7-(4-carboxybutanamido)cephalosporanate + H2O = (7R)-7-aminocephalosporanate + glutarate
For diagram of cephalosporin biosynthesis, click here
Other name(s): 7β-(4-carboxybutanamido)cephalosporanic acid acylase; cephalosporin C acylase; glutaryl-7-ACA acylase; CA; GCA; GA; cephalosporin acylase; glutaryl-7-aminocephalosporanic acid acylase; GL-7-ACA acylase
Systematic name: (7R)-7-(4-carboxybutanamido)cephalosporanate amidohydrolase
Comments: Forms 7-aminocephalosporanic acid, a key intermediate in the synthesis of cephem antibiotics. It reacts only weakly with cephalosporin C.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 56645-46-6
References:
1.  Ishii, Y., Saito, Y., Fujimura, T., Sasaki, H., Noguchi, Y., Yamada, H., Niwa, M. and Shimomura, K. High-level production, chemical modification and site-directed mutagenesis of a cephalosporin C acylase from Pseudomonas strain N176. Eur. J. Biochem. 230 (1995) 773–778. [DOI] [PMID: 7607251]
2.  Kinoshita, T., Tada, T., Saito, Y., Ishii, Y., Sato, A. and Murata, M. Crystallization and preliminary X-ray analysis of cephalosporin C acylase from Pseudomonas sp. strain N176. Acta Crystallogr. D Biol. Crystallogr. 56 (2000) 458–459. [PMID: 10739919]
3.  Monti, D., Carrea, G., Riva, S., Baldaro, E. and Frare, G. Characterization of an industrial biocatalyst: immobilized glutaryl-7-ACA acylase. Biotechnol. Bioeng. 70 (2000) 239–244. [PMID: 10972935]
4.  Kwon, T.H., Rhee, S., Lee, Y.S., Park, S.S. and Kim, K.H. Crystallization and preliminary X-Ray diffraction analysis of glutaryl-7-aminocephalosporanic acid acylase from Pseudomonas sp. GK16. J. Struct. Biol. 131 (2000) 79–81. [DOI] [PMID: 10945972]
5.  Kim, Y., Yoon, K.-H., Khang, Y., Turley, S. and Hol, W.G.J. The 2.0 Å crystal structure of cephalosporin acylase. Structure 8 (2000) 1059–1068. [DOI] [PMID: 11080627]
6.  Huang, X., Zeng, R., Ding, X., Mao, X., Ding, Y., Rao, Z., Xie, Y., Jiang, W. and Zhao, G. Affinity alkylation of the Trp-B4 residue of the β-subunit of the glutaryl 7-aminocephalosporanic acid acylase of Pseudomonas sp. 130. J. Biol. Chem. 277 (2002) 10256–10264. [DOI] [PMID: 11782466]
7.  Kim, J.K., Yang, I.S., Rhee, S., Dauter, Z., Lee, Y.S., Park, S.S. and Kim, K.H. Crystal structures of glutaryl 7-aminocephalosporanic acid acylase: insight into autoproteolytic activation. Biochemistry 42 (2003) 4084–4093. [DOI] [PMID: 12680762]
[EC 3.5.1.93 created 2005]
 
 
EC 3.5.1.94     
Accepted name: γ-glutamyl-γ-aminobutyrate hydrolase
Reaction: 4-(γ-L-glutamylamino)butanoate + H2O = 4-aminobutanoate + L-glutamate
Glossary: 4-aminobutanoate = γ-aminobutyrate = GABA
Other name(s): γ-glutamyl-GABA hydrolase; PuuD; YcjL; 4-(γ-glutamylamino)butanoate amidohydrolase; 4-(L-γ-glutamylamino)butanoate amidohydrolase
Systematic name: 4-(γ-L-glutamylamino)butanoate amidohydrolase
Comments: Forms part of a putrescine-utilizing pathway in Escherichia coli, in which it has been hypothesized that putrescine is first glutamylated to form γ-glutamylputrescine, which is oxidized to 4-(γ-glutamylamino)butanal and then to 4-(γ-glutamylamino)butanoate. The enzyme can also catalyse the reactions of EC 3.5.1.35 (D-glutaminase) and EC 3.5.1.65 (theanine hydrolase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Kurihara, S., Oda, S., Kato, K., Kim, H.G., Koyanagi, T., Kumagai, H. and Suzuki, H. A novel putrescine utilization pathway involves γ-glutamylated intermediates of Escherichia coli K-12. J. Biol. Chem. 280 (2005) 4602–4608. [DOI] [PMID: 15590624]
[EC 3.5.1.94 created 2006, modified 2011]
 
 
EC 3.5.1.95     
Accepted name: N-malonylurea hydrolase
Reaction: 3-oxo-3-ureidopropanoate + H2O = malonate + urea
For pyrimidine catabolism, click here
Other name(s): ureidomalonase
Systematic name: 3-oxo-3-ureidopropanoate amidohydrolase (urea- and malonate-forming)
Comments: Forms part of the oxidative pyrimidine-degrading pathway in some microorganisms, along with EC 1.17.99.4 (uracil/thymine dehydrogenase) and EC 3.5.2.1 (barbiturase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 368888-22-6
References:
1.  Soong, C.L., Ogawa, J. and Shimizu, S. Novel amidohydrolytic reactions in oxidative pyrimidine metabolism: analysis of the barbiturase reaction and discovery of a novel enzyme, ureidomalonase. Biochem. Biophys. Res. Commun. 286 (2001) 222–226. [DOI] [PMID: 11485332]
2.  Soong, C.L., Ogawa, J., Sakuradani, E. and Shimizu, S. Barbiturase, a novel zinc-containing amidohydrolase involved in oxidative pyrimidine metabolism. J. Biol. Chem. 277 (2002) 7051–7058. [DOI] [PMID: 11748240]
[EC 3.5.1.95 created 2006]
 
 
EC 3.5.1.96     
Accepted name: succinylglutamate desuccinylase
Reaction: N-succinyl-L-glutamate + H2O = succinate + L-glutamate
For diagram of arginine catabolism, click here
Other name(s): N2-succinylglutamate desuccinylase; SGDS; AstE
Systematic name: N-succinyl-L-glutamate amidohydrolase
Comments: Requires Co2+ for maximal activity [1]. N2-Acetylglutamate is not a substrate. This is the final enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine [1]. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. The five enzymes involved in this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.11 (acetylornithine transaminase), EC 1.2.1.71 (succinylglutamate-semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate desuccinylase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 99676-40-1
References:
1.  Vander Wauven, C. and Stalon, V. Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia. J. Bacteriol. 164 (1985) 882–886. [PMID: 2865249]
2.  Cunin, R., Glansdorff, N., Pierard, A. and Stalon, V. Biosynthesis and metabolism of arginine in bacteria. Microbiol. Rev. 50 (1986) 314–352. [PMID: 3534538]
3.  Cunin, R., Glansdorff, N., Pierard, A. and Stalon, V. Erratum report: Biosynthesis and metabolism of arginine in bacteria. Microbiol. Rev. 51 (1987) 178. [PMID: 16350242]
4.  Itoh, Y. Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa. J. Bacteriol. 179 (1997) 7280–7290. [DOI] [PMID: 9393691]
5.  Schneider, B.L., Kiupakis, A.K. and Reitzer, L.J. Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli. J. Bacteriol. 180 (1998) 4278–4286. [PMID: 9696779]
[EC 3.5.1.96 created 2006]
 
 
EC 3.5.1.97     
Accepted name: acyl-homoserine-lactone acylase
Reaction: an N-acyl-L-homoserine lactone + H2O = L-homoserine lactone + a carboxylate
Other name(s): acyl-homoserine lactone acylase; AHL-acylase; AiiD; N-acyl-homoserine lactone acylase; PA2385 protein; quorum-quenching AHL acylase; quorum-quenching enzyme; QuiP
Systematic name: N-acyl-L-homoserine-lactone amidohydrolase
Comments: Acyl-homoserine lactones (AHLs) are produced by a number of bacterial species and are used by them to regulate the expression of virulence genes in a process known as quorum-sensing. Each bacterial cell has a basal level of AHL and, once the population density reaches a critical level, it triggers AHL-signalling which, in turn, initiates the expression of particular virulence genes. Plants or animals capable of degrading AHLs would have a therapeutic advantage in avoiding bacterial infection as they could prevent AHL-signalling and the expression of virulence genes in quorum-sensing bacteria. This quorum-quenching enzyme removes the fatty-acid side chain from the homoserine lactone ring of AHL-dependent quorum-sensing signal molecules. It has broad specificity for AHLs with side changes ranging in length from 11 to 14 carbons. Substituents at the 3′-position, as found in N-(3-oxododecanoyl)-L-homoserine lactone, do not affect this activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Lin, Y.H., Xu, J.L., Hu, J., Wang, L.H., Ong, S.L., Leadbetter, J.R. and Zhang, L.H. Acyl-homoserine lactone acylase from Ralstonia strain XJ12B represents a novel and potent class of quorum-quenching enzymes. Mol. Microbiol. 47 (2003) 849–860. [DOI] [PMID: 12535081]
2.  Sio, C.F., Otten, L.G., Cool, R.H., Diggle, S.P., Braun, P.G., Bos, R., Daykin, M., Cámara, M., Williams, P. and Quax, W.J. Quorum quenching by an N-acyl-homoserine lactone acylase from Pseudomonas aeruginosa PAO1. Infect. Immun. 74 (2006) 1673–1682. [DOI] [PMID: 16495538]
[EC 3.5.1.97 created 2007]
 
 
EC 3.5.1.98     
Accepted name: histone deacetylase
Reaction: Hydrolysis of an N6-acetyl-lysine residue of a histone to yield a deacetylated histone
Other name(s): HDAC
Systematic name: histone amidohydrolase
Comments: A class of enzymes that remove acetyl groups from N6-acetyl-lysine residues on a histone. The reaction of this enzyme is opposite to that of EC 2.3.1.48, histone acetyltransferase. Histone deacetylases (HDACs) can be organized into three classes, HDAC1, HDAC2 and HDAC3, depending on sequence similarity and domain organization. Histone acetylation plays an important role in regulation of gene expression. In eukaryotes, HDACs play a key role in the regulation of transcription and cell proliferation [4]. May be identical to EC 3.5.1.17, acyl-lysine deacylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Krieger, D.E., Levine, R., Merrifield, R.B., Vidali, G. and Allfrey, V.G. Chemical studies of histone acetylation. Substrate specificity of a histone deacetylase from calf thymus nuclei. J. Biol. Chem. 249 (1974) 332–334. [PMID: 4855628]
2.  Sanchez del Pino, M.M., Lopez-Rodas, G., Sendra, R. and Tordera, V. Properties of the yeast nuclear histone deacetylase. Biochem. J. 303 (1994) 723–729. [PMID: 7980438]
3.  Ouaissi, M. and Ouaissi, A. Histone deacetylase enzymes as potential drug targets in cancer and parasitic diseases. J. Biomed. Biotechnol. 2006 (2006) 13474. [DOI] [PMID: 16883049]
4.  Song, Y.M., Kim, Y.S., Kim, D., Lee, D.S. and Kwon, H.J. Cloning, expression, and biochemical characterization of a new histone deacetylase-like protein from Thermus caldophilus GK24. Biochem. Biophys. Res. Commun. 361 (2007) 55–61. [DOI] [PMID: 17632079]
5.  Finnin, M.S., Donigian, J.R., Cohen, A., Richon, V.M., Rifkind, R.A., Marks, P.A., Breslow, R. and Pavletich, N.P. Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors. Nature 401 (1999) 188–193. [DOI] [PMID: 10490031]
6.  Phiel, C.J., Zhang, F., Huang, E.Y., Guenther, M.G., Lazar, M.A. and Klein, P.S. Histone deacetylase is a direct target of valproic acid, a potent anticonvulsant, mood stabilizer, and teratogen. J. Biol. Chem. 276 (2001) 36734–36741. [DOI] [PMID: 11473107]
7.  de Ruijter, A.J., van Gennip, A.H., Caron, H.N., Kemp, S. and van Kuilenburg, A.B. Histone deacetylases (HDACs): characterization of the classical HDAC family. Biochem. J. 370 (2003) 737–749. [DOI] [PMID: 12429021]
[EC 3.5.1.98 created 2008]
 
 
EC 3.5.1.99     
Accepted name: fatty acid amide hydrolase
Reaction: (1) anandamide + H2O = arachidonic acid + ethanolamine
(2) oleamide + H2O = oleic acid + NH3
Glossary: anandamide = (5Z,8Z,11Z,14Z)-N-(2-hydroxyethyl)icosa-5,8,11,14-tetraenamide
Other name(s): FAAH; oleamide hydrolase; anandamide amidohydrolase
Systematic name: fatty acylamide amidohydrolase
Comments: Integral membrane protein, the enzyme is responsible for the catabolism of neuromodulatory fatty acid amides, including anandamide and oleamide, occurs in mammalia.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Boger, D.L., Fecik, R.A., Patterson, J.E., Miyauchi, H., Patricelli, M.P. and Cravatt, B.F. Fatty acid amide hydrolase substrate specificity. Bioorg. Med. Chem. Lett. 10 (2000) 2613–2616. [DOI] [PMID: 11128635]
2.  Patricelli, M.P., Lashuel, H.A., Giang, D.K., Kelly, J.W. and Cravatt, B.F. Comparative characterization of a wild type and transmembrane domain-deleted fatty acid amide hydrolase: identification of the transmembrane domain as a site for oligomerization. Biochemistry 37 (1998) 15177–15187. [DOI] [PMID: 9790682]
3.  Patricelli, M.P. and Cravatt, B.F. Characterization and manipulation of the acyl chain selectivity of fatty acid amide hydrolase. Biochemistry 40 (2001) 6107–6115. [DOI] [PMID: 11352748]
[EC 3.5.1.99 created 2009]
 
 
EC 3.5.1.100     
Accepted name: (R)-amidase
Reaction: (1) (R)-piperazine-2-carboxamide + H2O = (R)-piperazine-2-carboxylate + NH3
(2) β-alaninamide + H2O = β-alanine + NH3
Other name(s): R-stereospecific amidase; R-amidase
Systematic name: (R)-piperazine-2-carboxamide amidohydrolase
Comments: In addition (R)-piperidine-3-carboxamide is hydrolysed to (R)-piperidine-3-carboxylic acid and NH3, and (R)-N-tert-butylpiperazine-2-carboxamide is hydrolysed to (R)-piperazine-2-carboxylic acid and tert-butylamine with lower activity. The enzyme does not act on the other amide substrates which are hydrolysed by EC 3.5.1.4 (amidase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Komeda, H., Harada, H., Washika, S., Sakamoto, T., Ueda, M. and Asano, Y. A novel R-stereoselective amidase from Pseudomonas sp. MCI3434 acting on piperazine-2-tert-butylcarboxamide. Eur. J. Biochem. 271 (2004) 1580–1590. [DOI] [PMID: 15066183]
[EC 3.5.1.100 created 2009, modified 2011]
 
 


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